RNA aptamers targeted for human αA-crystallin do not bind αB-crystallin, and spare the α-crystallin domain.
Sign Up to like & getrecommendations! Published in 2017 at "Biochemical and biophysical research communications"
DOI: 10.1016/j.bbrc.2017.07.085
Abstract: The molecular chaperones, α-crystallins, belong to the small heat shock protein (sHSP) family and prevent the aggregation and insolubilization of client proteins. Studies in vivo have shown that the chaperone activity of the α-crystallins is raised… read more here.
Keywords: bind; rna aptamers; aptamers targeted; crystallin ... See more keywords
βγ-Crystallination Endows a Novel Bacterial Glycoside Hydrolase 64 with Ca2+-Dependent Activity Modulation
Sign Up to like & getrecommendations! Published in 2019 at "Journal of Bacteriology"
DOI: 10.1128/jb.00392-19
Abstract: We have biochemically and structurally characterized a novel glucanase from the less studied GH64 family in a bacterium significant for fermentation of carbohydrates into biofuels. This enzyme displays a peculiar property of being distally modulated… read more here.
Keywords: gh64; crystallination; activity; ca2 ... See more keywords
Differential Roles of Three α-Crystallin Domain-Containing sHsps of Beauveria bassiana in Asexual Development, Multiple Stress Tolerance and Virulence
Sign Up to like & getrecommendations! Published in 2022 at "International Journal of Molecular Sciences"
DOI: 10.3390/ijms23126717
Abstract: Small heat shock proteins (sHsps) containing conserved α-crystallin domain play important roles in many cellular processes, but little is known about the functions of sHsps in filamentous entomopathogens. Here, three sHsps of Hsp20, Hsp30a, and… read more here.
Keywords: beauveria bassiana; asexual development; virulence; tolerance ... See more keywords